Anti-Bacteria Fimbrin Monoclonal antibody (DMAB9426)

Mouse Anti-Bacteria Fimbrin Monoclonal antibody for WB Datasheet

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Host Species
Antibody Isotype
Species Reactivity
Fimbrin from Dictyostelium discoideum strain AX2-214


Alternative Names
Fimbrin (p67)

Product Background

Gene summary
PLS1 (Plastin 1) is a Protein Coding gene. Among its related pathways are Sertoli-Sertoli Cell Junction Dynamics. GO annotations related to this gene include calcium ion binding and actin filament binding. An important paralog of this gene is LCP1. Plastins are a family of actin-binding proteins that are conserved throughout eukaryote evolution and expressed in most tissues of higher eukaryotes. In humans, two ubiquitous plastin isoforms (L and T) have been identified. The protein encoded by this gene is a third distinct plastin isoform, which is specifically expressed at high levels in the small intestine. Alternatively spliced transcript variants varying in the 5' UTR, but encoding the same protein, have been found for this gene. A pseudogene of this gene is found on chromosome 11.
Antigen Description
Actin-bundling protein in the absence of calcium. Fimbrin is an actin cross-linking protein important in the formation of filopodia. Fimbrin belongs to the calponin homology (CH) domain superfamily of actin cross-linking proteins. Like other members of this superfamily, which include α-actinin, β-spectrin, dystrophin, ABP-120 and filamin, it has a conserved 27 kDa actin-binding domain that contains a tandem duplication of a sequence that is homologous to calponin. In addition to cross-linking actin filaments into bundles and networks, CH domains also bind intermediate filaments and some signal transduction proteins to the actin cytoskeleton. Structural comparison of actin filaments and fimbrin CH domain-decorated actin filaments has revealed changes in the actin structure due to fimbrin-mediated cross-linking that may affect the actin filaments" affinity for other actin-binding proteins and may be part of the regulation of the cytoskeleton itself.


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Renley, BA; Rybakova, IN; et al. Dystrophin binding to nonmuscle actin. CELL MOTILITY AND THE CYTOSKELETON 41:264-270(1998).
Kennedy, BJ; Novotny, LA; et al. Passive transfer of antiserum specific for immunogens derived from a nontypeable Haemophilus influenzae adhesin and lipoprotein D prevents otitis media after heterologous challenge. INFECTION AND IMMUNITY 68:2756-2765(2000).

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